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Crystal structure of chaetomium thermophilum NAA20 in complex with a bisubstrate analogue

Analyse Crystal structure of chaetomium thermophilum NAA20 in complex with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZMP
Type
protein
Length
388 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-terminal acetyltransferase-like protein; Cmc-met-asp-glu-leu
UniProt
G0SGG4
Ligands
CMC
Pockets
4 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BN-terminal acetyltransferase-like proteinprotein19031% helix, 29% strandG0SGG4
C, DCmc-met-asp-glu-leuprotein40% helix, 0% strand—

Ligands and binding sites

  • CMC · Carboxymethyl coenzyme *A · ligand · 2 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19420.810.8293CMC
21250.560.8324empty
31070.550.8425empty
42120.520.7726empty

Interfaces

3 interfaces between chains.

  • A–B · 551 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 490 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 480 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 6ZMP · Crystal structure of Chaetomium thermophilum Naa20 in complex with a bisubstrate analogue · the same entry in another collection · chain A against A, TM-score 1.00

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